BMRB Entry 16093

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PDB ID: 2kcq
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16093
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of protein SRU_2040 from Salinibacter ruber (strain DSM 13855). Northeast Structural Genomics Consortium target SrR106

Deposition date:

2008-12-28

Original release date:

2009-03-05

Authors:

Wu, Yibing; Eletsky, Alexander; Zhao, Li; Hua, Jia; Sukumaran, Dinesh; Jiang, Mei; Foote, Erica; Xiao, Rong; Nair, Rajesh; Everett, John; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; SZYPERSKI, THOMAS

Citation:

Citation: Wu, Yibing; Eletsky, Alexander; Zhao, Li; Hua, Jia; Sukumaran, Dinesh; Jiang, Mei; Foote, Erica; Xiao, Rong; Nair, Rajesh. "Solution structure of protein SRU_2040 from Salinibacter ruber (strain DSM 13855) . Northeast Structural Genomics Consortium target SrR106" .

Assembly members:

Assembly members:
SRU_2040, polymer, 153 residues, 17088.771 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET 21-23C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SRU_2040: MKTTPDILDQIRVHGADAYP EEGCGFLLGTVTDDGDNRVA ALHRATNRRSEQRTRRYELT ADDYRAADAAAQEQGLDVVG VYHSHPDHPARPSATDLEEA TFPGFTYVIVSVRDGAPEAL TAWALAPDRSEFHREDIVRP DPEAPLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	431
15N chemical shifts	131
1H chemical shifts	895

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SRU_2040	1

Entities:

Entity 1, SRU_2040 153 residues - 17088.771 Da.

1

MET

LYS

THR

PRO

ASP

ILE

LEU

ASP

GLN

2

ILE

ARG

VAL

HIS

GLY

ALA

ASP

ALA

TYR

PRO

3

GLU

GLY

CYS

GLY

PHE

LEU

GLY

THR

4

VAL

THR

ASP

GLY

ASP

ASN

ARG

VAL

ALA

5

ALA

LEU

HIS

ARG

ALA

THR

ASN

ARG

SER

6

GLU

GLN

ARG

THR

ARG

TYR

GLU

LEU

THR

7

ALA

ASP

TYR

ARG

ALA

ASP

ALA

8

ALA

GLN

GLU

GLN

GLY

LEU

ASP

VAL

GLY

9

VAL

TYR

HIS

SER

HIS

PRO

ASP

HIS

PRO

ALA

10

ARG

PRO

SER

ALA

THR

ASP

LEU

GLU

ALA

11

THR

PHE

PRO

GLY

PHE

THR

TYR

VAL

ILE

VAL

12

SER

VAL

ARG

ASP

GLY

ALA

PRO

GLU

ALA

LEU

13

THR

ALA

TRP

ALA

LEU

ALA

PRO

ASP

ARG

SER

14

GLU

PHE

HIS

ARG

GLU

ASP

ILE

VAL

ARG

PRO

15

ASP

PRO

GLU

ALA

PRO

LEU

GLU

HIS

16

HIS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.7 mM; MES 20 mM; NACL 100 mM; CaCl2 5.0 mM; DTT 10 mM; NaN3 5%; D2O 10%; Protease Inhibitors 1

sample_2: entity, [U-5% 13C; U-99% 15N], 1.0 mM; MES 20 mM; NACL 100 mM; CaCl2 5.0 mM; DTT 10 mM; NaN3 5%; D2O 5%; Protease Inhibitors 1

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1.0 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
(4,3)D HABCAB(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
(4,3)D HCCH	sample_1	isotropic	sample_conditions_1
(N15-H1, C13-H1) simNOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1

Software:

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

AutoStruct, Huang, Tejero, Powers and Montelione - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

XEASY, Bartels et al. - peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Varian INOVA 750 MHz
Varian INOVA 600 MHz

PDB	2KCQ
EMBL	CBH25176
GB	ABC44045
REF	WP_011404768 YP_446146